1DVE

CRYSTAL STRUCTURE OF RAT HEME OXYGENASE-1 IN COMPLEX WITH HEME

Summary for 1DVE

• Entry DOI: 10.2210/pdb1dve/pdb
• Related: 1DVG 1QQ8
• Descriptor: HEME OXYGENASE-1, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: all alpha, protein-substrate complex, oxidoreductase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Microsome: P06762
• Total number of polymer chains: 1
• Total formula weight: 31228.98

Authors

Sugishima, M.,Omata, Y.,Kakuta, Y.,Sakamoto, H.,Noguchi, M.,Fukuyama, K. (deposition date: 2000-01-20, release date: 2000-04-12, Last modification date: 2024-02-07)

Primary citation

Sugishima, M.,Omata, Y.,Kakuta, Y.,Sakamoto, H.,Noguchi, M.,Fukuyama, K.
Crystal structure of rat heme oxygenase-1 in complex with heme.
FEBS Lett., 471:61-66, 2000

PubMed Abstract: Heme oxygenase catalyzes the oxidative cleavage of protoheme to biliverdin, the first step of heme metabolism utilizing O(2) and NADPH. We determined the crystal structures of rat heme oxygenase-1 (HO-1)-heme and selenomethionyl HO-1-heme complexes. Heme is sandwiched between two helices with the delta-meso edge of the heme being exposed to the surface. Gly143N forms a hydrogen bond to the distal ligand of heme, OH(-). The distance between Gly143N and the ligand is shorter than that in the human HO-1-heme complex. This difference may be related to a pH-dependent change of the distal ligand of heme. Flexibility of the distal helix may control the stability of the coordination of the distal ligand to heme iron. The possible role of Gly143 in the heme oxygenase reaction is discussed.

PubMed: 10760513
DOI: 10.1016/S0014-5793(00)01353-3

Experimental method

X-RAY DIFFRACTION (2.4 Å)